ID M0DE51_9EURY Unreviewed; 1081 AA.
AC M0DE51;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Signal-transducing histidine kinase {ECO:0000313|EMBL:ELZ33755.1};
GN ORFNames=C473_06745 {ECO:0000313|EMBL:ELZ33755.1};
OS Halorubrum terrestre JCM 10247.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum; Halorubrum distributum group.
OX NCBI_TaxID=1227486 {ECO:0000313|EMBL:ELZ33755.1, ECO:0000313|Proteomes:UP000011572};
RN [1] {ECO:0000313|EMBL:ELZ33755.1, ECO:0000313|Proteomes:UP000011572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10247 {ECO:0000313|EMBL:ELZ33755.1,
RC ECO:0000313|Proteomes:UP000011572};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELZ33755.1}.
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DR EMBL; AOIW01000044; ELZ33755.1; -; Genomic_DNA.
DR AlphaFoldDB; M0DE51; -.
DR PATRIC; fig|1227486.3.peg.1269; -.
DR Proteomes; UP000011572; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08448; PAS_4; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ELZ33755.1};
KW Transferase {ECO:0000313|EMBL:ELZ33755.1}.
FT DOMAIN 322..373
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 859..1069
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1081 AA; 117463 MW; 969AE7DA83611986 CRC64;
MDDPWGELPE PTRVRRASDG GSGATGESDS DGGPERLVVR LREDGDDGGA SGQSGSGRAN
ADLAAGDGAV ATDGLRALCD RYPDATILAY TVDDAPDAAI DASRLGVEYV SGRRLAADGE
TLADRLAERA GAGEAGDGRE RALESGAEAA SVLEPFIRIV SDRATDLDEK LDALLELGRD
RLGLSIGYSS HVDGDRLEIR QYSDGTGMLD ALLENNPDAD RSIPLELTYC QQTVRGDDVV
AFTDPEAAGL ADDPAYERFG FGSYVGGSVV VDDAVFGSLC FLDPERRDRP FDESERLFVE
LLADWLGRAI EREIAREERE AAVERFEETL ERIDDAFFAL DDDWRFTYVN EKAAALLDRQ
PDELLGADVW AEFPAAIGEE YETNYRRAME TQESVSFESY YEPLDLWTEV TAYPSPDGLS
VFFADATERK RRERVLERLL GTVEALQRTD SREAVADRLI GAADEILGHE ISGVRLYDPD
DDRLRLVATS DGLGERFADS RGPRRPGEGF TGRVFERGEP RVEEDISAAG DDRPYHGMRS
VAAVPLGDHG VFIVGAVDPD AFDESDVSVL ELLAANAVAA MDAADRRRRL RTYEDALKNV
DDMVCVLDGD GAVTYATGPF VSWIGADDLG DVAGRPLDAL VDEADAPRVA DAVAALTDAA
TEAGGAPEPT RTVDLTADRD GDRRSRHGEL RLSRLSDHGA GVVGSLSDTT DLRRTRTELS
AERDRFRRLF DRIPDPVIEV VLEPEETVID GANPAFEAQF GVDETTLRGR TIDALDIHDD
RLGDREGRGG VGAADLDSLV RERGFATEEV RRRTVDGPRE FLFRGFSYET EGTRRAFGIY
TDITDRKRRE RYVRIVNRIL RHNLRNELNV VFGFAGEIAD RTDDDMVRDF ARRIEATGKR
LSGVAEGAAT LRRVVEKGYA TDPEPIDVGA VVEEVVTRHA ADRPDARITA DVPAGIAVRG
DDRLSIAVDH LVENAVEHGG DAPRVAVTAE RDPDNGVVAV RVADDGPGIP TAVQEVITGT
REVTQLQHNT GVGLWIAAWV VEAYGGEIRF DDGLDGGGTT VTLVLPATER GGSGFDGESE
R
//
